SMART: Pfam domain GRASP55

The domain within your query sequence starts at position 49 and ends at position 185; the E-value for the GRASP55_65 domain shown below is 1.9e-65.

MLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAG
LRPHSDYIIGADTVMNESEDLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEG
SLGCGIGYGYLHRIPTR

GRASP55_65

PFAM accession number:	PF04495
Interpro abstract (IPR024958):	The Golgi apparatus is a highly dynamic organelle responsible for sorting out proteins and other biomolecules to the cell surface and to the extracellular milieu. The Golgi apparatus is comprised of flattened membrane-bound compartments called cisternae, which are apposed to one another to form a Golgi stack. The structural organization of the cisternae into stacks and their lateral connection, building the Golgi ribbon, requires a family of proteins called Golgi ReAssembly and Stacking Proteins (GRASP). Two homologues (GRASP55 and GRASP65) have been described in vertebrates and their functions have been associated to Golgi phosphorylation-regulated assembly/disassembly, protein secretion Golgi remodeling in migrating cells, among others. There is only one gene for GRASP in lower eukaryotes. Essentially all GRASPs contain a conserved N-terminal GRASP region, which comprises two tandem PDZ domains (PDZ1 and PDZ2), a classical protein-peptide interaction domain, and is responsible for GRASP homo-oligomerization and for the attachment to the Golgi membrane. The C-terminal half which is not conserved between species but is rich in proline and serines residues, as well as glutamine and asparagine residues [ (PUBMED:27436376) (PUBMED:21235525) (PUBMED:23940043) (PUBMED:21515684) ]. The GRASP-type PDZ domains adopt a canonical PDZ fold with a beta-sandwich of five beta-strands and two alpha-helices. The PDZ1 and PDZ2 domains are nearly superimposable. The peptide-binding pockets of both PDZ domains are formed by alpha2 and beta5. A typical ligand peptide is predicted to form antiparallel beta-strand interactions with beta5 and insert hydrophobic side chains between alpha2 and beta5. The two PDZ domains cooperate to achieve dimerization and oligomerization. In the dimers the PDZ2 domains interact in a way that positions the peptide-binding pockets facing each other. In addition, the dimers are linked through interactions between the two C-terminal tails (CTs) of one dimer and two peptide-binding pockets of the PDZ1 domains in the next dimer [ (PUBMED:23940043) (PUBMED:21515684) ]. This entry represents the GRASP-type PDZ domain.

PFAM accession number:

PF04495

Interpro abstract (IPR024958):

The Golgi apparatus is a highly dynamic organelle responsible for sorting out proteins and other biomolecules to the cell surface and to the extracellular milieu. The Golgi apparatus is comprised of flattened membrane-bound compartments called cisternae, which are apposed to one another to form a Golgi stack. The structural organization of the cisternae into stacks and their lateral connection, building the Golgi ribbon, requires a family of proteins called Golgi ReAssembly and Stacking Proteins (GRASP). Two homologues (GRASP55 and GRASP65) have been described in vertebrates and their functions have been associated to Golgi phosphorylation-regulated assembly/disassembly, protein secretion Golgi remodeling in migrating cells, among others. There is only one gene for GRASP in lower eukaryotes. Essentially all GRASPs contain a conserved N-terminal GRASP region, which comprises two tandem PDZ domains (PDZ1 and PDZ2), a classical protein-peptide interaction domain, and is responsible for GRASP homo-oligomerization and for the attachment to the Golgi membrane. The C-terminal half which is not conserved between species but is rich in proline and serines residues, as well as glutamine and asparagine residues [ (PUBMED:27436376) (PUBMED:21235525) (PUBMED:23940043) (PUBMED:21515684) ].

The GRASP-type PDZ domains adopt a canonical PDZ fold with a beta-sandwich of five beta-strands and two alpha-helices. The PDZ1 and PDZ2 domains are nearly superimposable. The peptide-binding pockets of both PDZ domains are formed by alpha2 and beta5. A typical ligand peptide is predicted to form antiparallel beta-strand interactions with beta5 and insert hydrophobic side chains between alpha2 and beta5. The two PDZ domains cooperate to achieve dimerization and oligomerization. In the dimers the PDZ2 domains interact in a way that positions the peptide-binding pockets facing each other. In addition, the dimers are linked through interactions between the two C-terminal tails (CTs) of one dimer and two peptide-binding pockets of the PDZ1 domains in the next dimer [ (PUBMED:23940043) (PUBMED:21515684) ].

This entry represents the GRASP-type PDZ domain.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GRASP55_65